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Database: UniProt
Entry: B6QQG3_TALMQ
LinkDB: B6QQG3_TALMQ
Original site: B6QQG3_TALMQ 
ID   B6QQG3_TALMQ            Unreviewed;       327 AA.
AC   B6QQG3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Aha1 domain family {ECO:0000313|EMBL:EEA20277.1};
GN   ORFNames=PMAA_041300 {ECO:0000313|EMBL:EEA20277.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA20277.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|EMBL:EEA20277.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 18224 {ECO:0000313|EMBL:EEA20277.1};
RA   Zhao H., Waite J.H.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SIMILARITY: Belongs to the AHA1 family.
CC       {ECO:0000256|ARBA:ARBA00006817}.
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DR   EMBL; DS995904; EEA20277.1; -; Genomic_DNA.
DR   EMBL; DS995904; EEA20278.1; -; Genomic_DNA.
DR   RefSeq; XP_002151277.1; XM_002151241.1.
DR   RefSeq; XP_002151278.1; XM_002151242.1.
DR   AlphaFoldDB; B6QQG3; -.
DR   VEuPathDB; FungiDB:PMAA_041300; -.
DR   HOGENOM; CLU_049046_1_0_1; -.
DR   OrthoDB; 5473696at2759; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   CDD; cd08892; SRPBCC_Aha1; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   Gene3D; 3.15.10.20; Activator of Hsp90 ATPase Aha1, N-terminal domain; 1.
DR   InterPro; IPR036338; Aha1.
DR   InterPro; IPR015310; AHSA1-like_N.
DR   InterPro; IPR013538; ASHA1-like_C.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   PANTHER; PTHR13009; HEAT SHOCK PROTEIN 90 HSP90 CO-CHAPERONE AHA-1; 1.
DR   PANTHER; PTHR13009:SF8; LD43819P; 1.
DR   Pfam; PF09229; Aha1_N; 1.
DR   Pfam; PF08327; AHSA1; 1.
DR   SMART; SM01000; Aha1_N; 1.
DR   SUPFAM; SSF103111; Activator of Hsp90 ATPase, Aha1; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT   DOMAIN          13..146
FT                   /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01000"
FT   REGION          145..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   327 AA;  36366 MW;  1E82F5416E15B46B CRC64;
     MALHNPNNWH WVNKDVSPWT KTYLQDSLSK ISAEENGVSA KVEKVLSMDG DVDVSQRKGK
     VITLYDVKLQ LEYEGKTKDE ETVTGTITIP EVAHDTEEDE FVFEISVYSE SSSKQPVKDL
     VRSKIVPQLR VALAKLPQVL VSEHGKDIQH APGSNPSSGF ATPAYHPQKS SSPAVGTSKT
     TTTSTGKVSV NTTTVTASDE FRTTAEELYT TFTDPQRIAA FTRGPPLQFD GAKVGGKFAI
     FDGNVTGEYV TLEPFKRVVQ KWRLAQWPEG HFSTQEIVFN QNDVDRVTVM QVTWTGVPIG
     QEEVVQRNWE GYYVRSIKQT FGFGTIL
//
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